Properties of the ribosome-inactivating proteins gelonin, Momordica charantia inhibitor, and dianthins

Biochem J. 1982 Dec 1;207(3):505-9. doi: 10.1042/bj2070505.

Abstract

The amino acid and sugar compositions of four ribosome-inactivating proteins (gelonin, Momordica charantia inhibitor, dianthin 30 and dianthin 32) were determined. The proteins are all basic glycoproteins (pI greater than 8) containing mannose (more abundant in gelonin), glucose, xylose, fucose (absent from gelonin) and glucosamine. The ribosome-inactivating properties of the proteins examined are not modified by pretreatment with N-ethylmaleimide. Precipitating and inactivating antibodies can be raised against ribosome-inactivating proteins; a weak cross-reaction was observed only between dianthin 30 and dianthin 32.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acids / analysis
  • Animals
  • Antimetabolites / pharmacology*
  • Carbohydrates / analysis
  • Ethylmaleimide / pharmacology
  • Immunodiffusion
  • Isoelectric Point
  • N-Glycosyl Hydrolases*
  • Plant Proteins / pharmacology*
  • Rabbits
  • Ribosome Inactivating Proteins, Type 1
  • Ribosome Inactivating Proteins, Type 2
  • Ribosomes / drug effects*

Substances

  • Amino Acids
  • Antimetabolites
  • Carbohydrates
  • Plant Proteins
  • Ribosome Inactivating Proteins, Type 1
  • Ribosome Inactivating Proteins, Type 2
  • GEL protein, Gelonium multiflorum
  • N-Glycosyl Hydrolases
  • Ethylmaleimide